Altered muropeptide composition in Staphylococcus aureus strains with an inactivated femA locus

J Bacteriol. 1993 May;175(9):2779-82. doi: 10.1128/jb.175.9.2779-2782.1993.

Abstract

Tn551 inactivation of femA, a factor involved in methicillin resistance of Staphylococcus aureus, caused the production of peptidoglycan in which the fraction of monoglycyl- and serine-containing muropeptides was increased at the expense of pentaglycyl muropeptides. femA mutants have a specific block in the biosynthesis of pentaglycine cross bridges after the addition of the first glycine residue.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cell Wall / chemistry*
  • Cell Wall / metabolism
  • Genes, Bacterial / genetics
  • Glycine / analysis
  • Molecular Sequence Data
  • Muramic Acids / chemistry*
  • Muramic Acids / metabolism
  • Mutagenesis, Insertional
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism
  • Peptidoglycan / chemistry*
  • Peptidoglycan / metabolism
  • Protein Conformation
  • Serine / analysis
  • Staphylococcus aureus / chemistry*
  • Staphylococcus aureus / genetics

Substances

  • Muramic Acids
  • Oligopeptides
  • Peptidoglycan
  • Serine
  • Glycine